Effect of DTNB light chain on the interaction of vertebrate skeletal myosin with actin
Authors:
- Sarkis S. MargossianSMSarkis S. Margossian
- Susan LoweySLSusan Lowey
- Bruce BarshopBBBruce Barshop
- 1 November 1975
- journal article
- Published by Springer Nature in Nature
- Vol. 258 (5531) , 163-166
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- The effects of concentrated salt solutions on the structure and the enzymatic activity of myosin molecules from skeletal and cardiac musclesFEBS Letters, 1975
- X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscleJournal of Molecular Biology, 1975
- Evidence for structural changes in vertebrate thick filaments induced by calciumJournal of Molecular Biology, 1974
- Substructure of the myosin moleculeJournal of Molecular Biology, 1973
- The light chains of scallop myosin as regulatory subunitsJournal of Molecular Biology, 1973
- Light Chains from Fast and Slow Muscle MyosinsNature, 1971
- Substructure of the myosin moleculeJournal of Molecular Biology, 1971
- Regulation in molluscan musclesJournal of Molecular Biology, 1970
- Relation of structure to function in myosin. II. Salt denaturation and recombination experimentsBiochemistry, 1970
- Evidence for the involvement of light chains in the biological functioning of myosinBiochemical and Biophysical Research Communications, 1969